Peptide amphiphile systems can seamlessly integrate sequence control and tunable secondary structure in one supramolecular system, making them ideal candidate for a selective, molecular-recognition material for phosphate. Compared to other anion-binding materials that are unstable in water and have complex synthetic routes, peptide amphiphiles function optimally in aqueous environments and use solid-phase peptide synthesis, a technique that is well-established and sequence-specific. For this application, phosphate binding sequences can be reliably incorporated directly into the peptide headgroup of the PA molecule, displaying the binding motif to the environment. In terms of micelle architectures, PAs possess the advantages of spontaneous self-assembly in water as well as reproducible tunability of the supramolecular structures formed. This paper will present results on phosphate binding by specially designed peptide amphiphiles.

Peptide amphiphiles for phosphate recovery

2019 Fall National Meeting

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